› 3ih7

X-ray diffraction
3.1Å resolution

Crystal structure of catalytically active human 8-oxoguanine glycosylase distally crosslinked to guanine-containing DNA

Released:
DOI: 10.2210/pdb3ih7/pdb
PDB entry 3ih7 coloured by chain, front view.
PDB entry 3ih7 coloured by chain, side view.
PDB entry 3ih7 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Verdine GL, Crenshaw CM, Oo KS, Kutchukian PS

Function and Biology Details

Reaction catalysed: 
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-116408 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
N-glycosylase/DNA lyase Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 35.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15527 (Residues: 12-325; Coverage: 91%)
Gene names: MMH, MUTM, OGG1, OGH1
Sequence domains:
Structure domains:
5'-D(*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*G)-3' Chain: B
Molecule details ›
Chain: B
Length: 14 nucleotides
Theoretical weight: 4.35 KDa
Source organism: Homo sapiens
Expression system: Not provided
5'-D(AP*TP*CP*TP*GP*GP*AP*CP*CP*TP*GP*CP*A)-3' Chain: C
Molecule details ›
Chain: C
Length: 13 nucleotides
Theoretical weight: 3.95 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P6522
Unit cell:
a: 91Å b: 91Å c: 211.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.228 0.267
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

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